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Transportation governed by simple rules
Date:5/3/2010

ene can be found in many tumours. However, it is only able to function fully when it is embedded in the cell membrane and does not get into any other membranes. So the scientists developed an inhibitor they called palmostatin B to counteract the enzyme responsible for detaching the lipid anchor. When the enzyme is switched off, the palmitoylated Ras remains embedded in the cell membrane, from whence it gets into the membrane of other cellular organelles. "This was a brand new approach and it actually goes against common sense. That's why it was never taken any further in pharmaceutical research. What we did was this: instead of inhibiting directed transportation from the Golgi apparatus, we promoted random distribution within the cell," explains Herbert Waldmann, Head of the Department of Chemical Biology at the Max Planck Institute in Dortmund.

For the first time ever, the scientists using palmostatin B were able to inhibit the Ras protein without switching it off completely. If Ras is completely inactivated, even healthy cells die. By contrast, random distribution within the cell suppresses only the harmful impact of the mutated Ras protein. Cancer cells thus become normal cells again. Thanks to this discovery, Ras-dependent tumours could one day be treated in a manner that does not damage healthy cells.


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Contact: Philippe Bastiaens
philippe.bastiaens@mpi-dortmund.mpg.de
49-023-113-32200
Max-Planck-Gesellschaft
Source:Eurekalert  

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